Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4XBI5 (GLMM_SALTO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Strop_3862
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000343596

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XBI5 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 7296D8CEE12160D2

FASTA45146,229
        10         20         30         40         50         60 
MGRLFGTDGV RGRANADLTP ELGLAVAVAA AHTLAEADRS HPPLAVVGRD TRASGEMLES 

        70         80         90        100        110        120 
AVVAGLTSAG ANVVRVGVLP TPAVAFLTAE AKADIGVMLS ASHNPMPDNG IKLFAAGGHK 

       130        140        150        160        170        180 
LPDEIEMKIE AAVEANTTTA WERPVGAGVG RVHDLLDGAD HYVQHLVGTV PHRLDGIKVV 

       190        200        210        220        230        240 
VDCANGAAAE VAPAAYREAG AEVVAIHAEP NGLNINDECG SNHVAALRQA VVEHGAQLGI 

       250        260        270        280        290        300 
AHDGDADRCV AVTADGDEVD GDQVMAILAL AMREAGTLTA DTLVATVMSN LGLRIAMSRE 

       310        320        330        340        350        360 
GIRLVETKVG DRYVLEELRA SGLALGGEQS GHIVMPAHAT TGDGVLTGLH LMSRMAGTGR 

       370        380        390        400        410        420 
PLAELAAVVS PLPQVLINVP VGDRTVGAAA PAVRAEVARA EAELGDAGRV LLRPSGTEPL 

       430        440        450 
VRVMVEAGTE TTAREVAERI AEQVRTASPV S 

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000667 Genomic DNA. Translation: ABP56292.1.
RefSeqYP_001160670.1. NC_009380.1.

3D structure databases

ProteinModelPortalA4XBI5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4XBI5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5060340.
GenomeReviewsGene locus Strop_3862 in contig CP000667_GR.
KEGGstp:Strop_3862.
PATRIC23446916. VBISalTro43511_3986.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBA4XBI5.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycSTRO369723:STROP_3862-MONOMER.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[Tree]
InterProIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_SALTO
AccessionPrimary (citable) accession number: A4XBI5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 29, 2007
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families